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Magnesium in PDB 5g2r: Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana

Enzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana

All present enzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana:
2.10.1.1;

Protein crystallography data

The structure of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana, PDB code: 5g2r was solved by J.Krausze, S.Saha, C.Probst, T.Kruse, D.W.Heinz, R.R.Mendel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.940 / 2.45
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 65.880, 123.410, 130.450, 90.00, 90.00, 90.00
R / Rfree (%) 23.33 / 25.44

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana (pdb code 5g2r). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana, PDB code: 5g2r:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5g2r

Go back to Magnesium Binding Sites List in 5g2r
Magnesium binding site 1 out of 2 in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1500

b:40.6
occ:1.00
O A:HOH2040 2.0 48.1 1.0
O A:HOH2042 2.0 69.4 1.0
O A:HOH2059 2.1 50.5 1.0
O A:HOH2028 2.1 51.4 1.0
O A:HOH2027 2.1 60.2 1.0
O A:HOH2058 2.1 68.2 1.0
OD1 A:ASP274 4.1 57.6 1.0
O A:HOH2044 4.2 46.7 1.0
OE2 A:GLU201 4.4 42.8 1.0
N A:GLY267 4.4 53.5 1.0
OD2 A:ASP242 4.5 52.9 1.0
OD1 A:ASP242 4.6 55.0 1.0
CA A:GLY199 4.7 48.6 1.0
O A:THR198 4.8 57.6 1.0
OE1 A:GLU201 4.8 47.5 1.0
CG A:ASP242 4.9 54.0 1.0
CA A:GLY267 5.0 53.5 1.0

Magnesium binding site 2 out of 2 in 5g2r

Go back to Magnesium Binding Sites List in 5g2r
Magnesium binding site 2 out of 2 in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1501

b:78.0
occ:0.50
OD1 A:ASP435 3.1 90.0 1.0
CG1 A:ILE436 4.1 83.7 1.0
N A:ILE436 4.2 89.9 1.0
CG A:ASP435 4.3 89.1 1.0
CA A:ASP435 4.3 85.1 1.0
CD2 A:LEU353 4.4 51.0 1.0
CD1 A:ILE436 4.6 83.4 1.0
CB A:ASP435 4.7 86.1 1.0
C A:ASP435 4.8 90.6 1.0

Reference:

J.Krausze, C.Probst, U.Curth, J.Reichelt, S.Saha, D.Schafflik, D.W.Heinz, R.R.Mendel, T.Kruse. Dimerization of the Plant Molybdenum Insertase CNX1E Is Required For Synthesis of the Molybdenum Cofactor. Biochem.J. V. 474 163 2017.
ISSN: ISSN 0264-6021
PubMed: 27803248
DOI: 10.1042/BCJ20160846
Page generated: Sun Sep 29 04:35:24 2024

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